ID A0A2T5XY18_9FLAO Unreviewed; 350 AA. AC A0A2T5XY18; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 03-AUG-2022, entry version 13. DE RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769}; DE Includes: DE RecName: Full=Diaminohydroxyphosphoribosylaminopyrimidine deaminase {ECO:0000256|PIRNR:PIRNR006769}; DE Short=DRAP deaminase {ECO:0000256|PIRNR:PIRNR006769}; DE EC=3.5.4.26 {ECO:0000256|PIRNR:PIRNR006769}; DE AltName: Full=Riboflavin-specific deaminase {ECO:0000256|PIRNR:PIRNR006769}; DE Includes: DE RecName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase {ECO:0000256|PIRNR:PIRNR006769}; DE EC=1.1.1.193 {ECO:0000256|PIRNR:PIRNR006769}; DE AltName: Full=HTP reductase {ECO:0000256|PIRNR:PIRNR006769}; GN ORFNames=C8P65_10182 {ECO:0000313|EMBL:PTX08418.1}; OS Capnocytophaga leadbetteri. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=327575 {ECO:0000313|EMBL:PTX08418.1, ECO:0000313|Proteomes:UP000243985}; RN [1] {ECO:0000313|EMBL:PTX08418.1, ECO:0000313|Proteomes:UP000243985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22902 {ECO:0000313|EMBL:PTX08418.1, RC ECO:0000313|Proteomes:UP000243985}; RA Goeker M.; RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II RT (KMG-II): from individual species to whole genera."; RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- CC phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- CC phosphate. {ECO:0000256|ARBA:ARBA00002151, CC ECO:0000256|PIRNR:PIRNR006769}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + CC H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+); CC Xref=Rhea:RHEA:21868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58453, ChEBI:CHEBI:58614; EC=3.5.4.26; CC Evidence={ECO:0000256|PIRNR:PIRNR006769}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5- CC amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH; CC Xref=Rhea:RHEA:17845, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58421, ChEBI:CHEBI:58453; CC EC=1.1.1.193; Evidence={ECO:0000256|PIRNR:PIRNR006769}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR006769, CC ECO:0000256|PIRSR:PIRSR006769-3}; CC Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769, CC ECO:0000256|PIRSR:PIRSR006769-3}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D- CC ribitylamino)uracil from GTP: step 2/4. {ECO:0000256|ARBA:ARBA00004882, CC ECO:0000256|PIRNR:PIRNR006769}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D- CC ribitylamino)uracil from GTP: step 3/4. {ECO:0000256|ARBA:ARBA00004910, CC ECO:0000256|PIRNR:PIRNR006769}. CC -!- SIMILARITY: In the C-terminal section; belongs to the HTP reductase CC family. {ECO:0000256|ARBA:ARBA00007417, ECO:0000256|PIRNR:PIRNR006769}. CC -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and CC deoxycytidylate deaminase family. {ECO:0000256|ARBA:ARBA00005259, CC ECO:0000256|PIRNR:PIRNR006769}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PTX08418.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QBKG01000001; PTX08418.1; -; Genomic_DNA. DR EnsemblBacteria; PTX08418; PTX08418; C8P65_10182. DR UniPathway; UPA00275; UER00401. DR Proteomes; UP000243985; Unassembled WGS sequence. DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_dom. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR024072; DHFR-like_dom_sf. DR InterPro; IPR004794; Eubact_RibD. DR InterPro; IPR002734; RibDG_C. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF01872; RibD_C; 1. DR PIRSF; PIRSF006769; RibD; 1. DR SUPFAM; SSF53597; SSF53597; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR00326; eubact_ribD; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|PIRNR:PIRNR006769}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR006769}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW NADP {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-2}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006769}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, KW ECO:0000256|PIRNR:PIRNR006769}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006769}. FT DOMAIN 1..125 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000259|PROSITE:PS51747" FT ACT_SITE 52 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-1" FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT BINDING 77 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT BINDING 156 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 175 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 201 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 205 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 209 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 212 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 291 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" SQ SEQUENCE 350 AA; 39328 MW; 4D22C58BDB4C1C54 CRC64; MTDQQYIHRC IQLAQNGLGT TYPNPVVGSV IVYKDRVIGE GWHVRAGEAH AEVRAIASVK DKQLLSQSTL YVSLEPCSHY GKTPPCADLI IAHRIPRVVI GCTDPFAKVA GRGIQKLREA GCEVVVGVCQ EECEALNKRF FTFHQKKRPY IFLKWAETRD GLIAPLHKQE RAPQWITGAY ARQYVHLLRS TEAAILVGAG TVWADNPSLS TRSWYGKSPL RVIIDPRLST RKDFNVWNDE VPTLFIADRD YKGVRHFGQR TEVACIDFGG EVLPQLCKVL YEREVQSLIV EGGAHTLQQF IKADLWDEAL VFRGDTVFTN GLKAPQLSHA CLHSVESFPP DFLMTMVNNK //